Advances in protein chemistry. / Volume by M L Anson; John T Edsall

By M L Anson; John T Edsall

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However, the optical data require only that the major axes of the submicroscopic protein components extend in planes paralleling that of the envelope. These components may as well be very thin fibrils, interlaced or oriented at random, as in nets or gridq. s (1941) favors the view that the envelope is composed of a lattice of thin protein fibrils with lipid molecules interspersed between the protein particles. The membranes of vacuoles have a similar structure. Schmidt (1939,c) observed changes in the birefringence of the contractile vacuole of Amoeba with the cyclic contraction and filling and suggested that the protein chains oriented parallel with the membrane of the vacuole are responsible for the contraction.

A change in distribution of water between polar groups in fibrous proteins and ionogenic groups in the environment appears to be a t the bottom of contractility generally. The submicroscopic longitudinal fibrils here described provide a unique capillary system in which a change in distribution of interfibrillary water might cause the undulatory contortions charac teristic of the sperm tail and the pendular beating of cilia and flagella. Since no formed structure other than the fibrils has been found, it may he supposed, for the present, that they not only furnish the rigidity and elasticity required but also play a rale in the events by which chemical energy from carbohydrate metabolism is converted into mechanical energy.

The authors are at pains to prove that the material comes only from the nucleus, which is generally considered to be the only source of thymonucleic acid. They state that histones or protamines constitute the sole protein component. The almost complete absence of tryptophan, which is found in most other proteins, is cited aa evidence for this view. 6 Stedman and Stedman (1948)believe that the above view of the composition of chromatin is erroneous. They state that the principal component of chromatin is an acidic protein to which they give the name chromosomin.

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